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Conserved domains on  [gi|2068726809|ref|XP_042207400|]
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laminin subunit alpha-2-like [Homarus americanus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1808-1963 2.26e-34

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


:

Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 129.85  E-value: 2.26e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1808 GSYFPGDAYAIYSDDFNVGSLLELRLEFRTWELNGIILSVADPRGTS-LSLELVNGAVLLTVDMGSGhpfsaRVRLRNKF 1886
Cdd:cd00110      1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDfLALELEDGRLVLRYDLGSG-----SLVLSSKT 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068726809 1887 NFCDNMWHTVKASYIKDSLSLRVDDYREAYGFNGSGNDERTLTGaPFYIGGLPDAALQGTLTARDNFKGCIRNIVLN 1963
Cdd:cd00110     76 PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDG-PLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
Laminin_B pfam00052
Laminin B (Domain IV);
107-244 1.26e-31

Laminin B (Domain IV);


:

Pssm-ID: 459652  Cd Length: 136  Bit Score: 121.22  E-value: 1.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  107 YWQLPRGFKRDKVTSYNGYLRFRVHSEGGNkifPDQILQSYPLVSLQGNwQLVLEYY-----PPAISTDGRYEVKLHEDY 181
Cdd:pfam00052    1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLP---GGGSLNSEPDVILEGN-GLRLSYSspdqpPPDPGQEQTYSVRLHEEN 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068726809  182 WRLKNKPQkVTREMMMIALQNIQHILIRATHAADATTASIHDVTLDVAAEGSpvSSRVALGVE 244
Cdd:pfam00052   77 WRDSDGAP-VSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGG--SGPPASWVE 136
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1388-1570 2.81e-27

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


:

Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 109.43  E-value: 2.81e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1388 AGFLGQGFVELP-SHILKRDSNFGFTFQTMEADALLMlstFIGQDNETDgdmstttttttttstptprqpgeehppdYYS 1466
Cdd:cd00110      2 VSFSGSSYVRLPtLPAPRTRLSISFSFRTTSPNGLLL---YAGSQNGGD----------------------------FLA 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1467 VSLVEGHLDIRLNGGTSSHRIMSSAKYNDGYLHSFFVIKENRRVTLKVDDKEVNGTRLDRGSQvvSGPDTGGLYFGGVPR 1546
Cdd:cd00110     51 LELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSA--LLNLDGPLYLGGLPE 128
                          170       180
                   ....*....|....*....|....
gi 2068726809 1547 DIEaVTMVGSSRSLKGCIRDVIIN 1570
Cdd:cd00110    129 DLK-SPGLPVSPGFVGCIRDLKVN 151
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1631-1780 2.23e-23

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


:

Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 98.26  E-value: 2.23e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1631 ESYVMVPlNSRTFKKNFTVSFEFRTYYPNGLFFivSNTRKKRTQTISAQLRNGRVIVSMEKeskkGPKNIEAASKPGLNT 1710
Cdd:cd00110      7 SSYVRLP-TLPAPRTRLSISFSFRTTSPNGLLL--YAGSQNGGDFLALELEDGRLVLRYDL----GSGSLVLSSKTPLND 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068726809 1711 GQWRKVMIEKFRKRLLLFIDNQLVKKEKAPRK---MNVGRELFLGSLPASDDNPDnMQETETLRGCLRNLKIN 1780
Cdd:cd00110     80 GQWHSVSVERNGRSVTLSVDGERVVESGSPGGsalLNLDGPLYLGGLPEDLKSPG-LPVSPGFVGCIRDLKVN 151
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1029-1168 2.21e-20

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


The actual alignment was detected with superfamily member pfam00054:

Pssm-ID: 473984 [Multi-domain]  Cd Length: 131  Bit Score: 88.91  E-value: 2.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1029 SERNALLVYLGTNNSSDYMAVEMVNRRIEFSWDAGGGAQRITHPLRLltstpyvnDDIRWYYISINRIGNIGQLSVtpan 1108
Cdd:pfam00054    4 TEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKL--------NDGKWHSVELERNGRSGTLSV---- 71
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068726809 1109 veeTGDEVGTIVSNASPAGFSKMDILpsdsLWVGGAPSNVSDLLKTN---KFSGCLHTLSIDG 1168
Cdd:pfam00054   72 ---DGEARPTGESPLGATTDLDVDGP----LYVGGLPSLGVKKRRLAispSFDGCIRDVIVNG 127
Laminin_I super family cl26988
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
457-700 2.32e-16

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


The actual alignment was detected with superfamily member pfam06008:

Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 80.92  E-value: 2.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  457 SINVTAyvpAPWPTIRELQNVTRILRYQLDRYHSNVDvSQELVVEFdLDYYSKDLKQRAEQLEAAARETYPPTAKLRLEA 536
Cdd:pfam06008    3 SLNSLT---GALPAPYKINYNLENLTKQLQEYLSPEN-AHKIQIEI-LEKELSSLAQETEELQKKATQTLAKAQQVNAES 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  537 QSILDILNGLYTQID----------ETIAYLkNYAIGETPSISIGGAMMEAEKILKEIQKRNFTKNDAEAKIELSKAHIL 606
Cdd:pfam06008   78 ERTLGHAKELAEAIKnlidnikeinEKVATL-GENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  607 LKRIMKMDQEH-----PLIEAGRTHIRDIENKLKELLQRIEAANRKTNEASELNKNNAKRLARVQTYSAEiknsryiIDN 681
Cdd:pfam06008  157 LSRIQTWFQSPqeenkALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEE-------VSE 229
                          250
                   ....*....|....*....
gi 2068726809  682 QNFNSTQLLKEANKNLINT 700
Cdd:pfam06008  230 QKNQLEETLKTARDSLDAA 248
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
288-337 1.27e-13

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 66.61  E-value: 1.27e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2068726809  288 CRCNGR---SETCDAETGVCEnCRDHTMGDHCEVCATGYYGNPArerCKPCAC 337
Cdd:pfam00053    1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS---DPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
389-434 4.51e-13

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 65.07  E-value: 4.51e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2068726809  389 PCDCDPFGSVHEGCDR-DGVCTCKPGITGRDCSQCASRHV---TSATGCR 434
Cdd:cd00055      1 PCDCNGHGSLSGQCDPgTGQCECKPNTTGRRCDRCAPGYYglpSQGGGCQ 50
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1228-1363 6.35e-13

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


:

Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 67.44  E-value: 6.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1228 FKTLDEDALLFLAVNEaKNQYFSISLDSGHVVFTVQFDPQTRLLMKSSKQLNNNED-MVQIqaivpnkERGGaRMGRLVV 1306
Cdd:pfam02210    1 FRTRQPNGLLLYAGGG-GSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWhSVRV-------ERNG-NTLTLSV 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2068726809 1307 GDQDQIGTVKGGPDLDL-SFVPYYFGGVDPEFnrgRWGSELVLRSLLGCMTGLSVLDE 1363
Cdd:pfam02210   72 DGQTVVSSLPPGESLLLnLNGPLYLGGLPPLL---LLPALPVRAGFVGCIRDVRVNGE 126
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
334-388 1.03e-09

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 55.82  E-value: 1.03e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2068726809  334 PCACPSleqNFAETCQADRYAGyICHCRTGYTGAKCNRCDHGYYGRPSQPRGyCR 388
Cdd:cd00055      1 PCDCNG---HGSLSGQCDPGTG-QCECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
Laminin_II super family cl05515
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ...
895-1019 1.08e-05

Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


The actual alignment was detected with superfamily member pfam06009:

Pssm-ID: 368703 [Multi-domain]  Cd Length: 138  Bit Score: 47.10  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  895 EETYSNVQKTLDHINAIHMNLTIIRERaleLSRIDASLlyeirETISTGESHTMKGIRKAN----NLRKTGDRI------ 964
Cdd:pfam06009    6 REANETAKEVLEQLAPLSQNLENTSEK---LSGINRSL-----EETNELVNDANKALDDAGrsvkKLEELAPDLldklkp 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2068726809  965 ----ENYSNDLRERIEALKRKIKQTRQYASSIRVSLttNSSGICTRKYRPalqPSTTTN 1019
Cdd:pfam06009   78 lkqlEVNSSSLSDNISRIKELIAQARKAANSIKVSV--SFDGDSIVELRP---PISVTD 131
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
624-984 3.63e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 3.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  624 RTHIRDIENKLKELLQRIEAANRKTNEASEL--NKNNAKRLARVQTYSAEIKnsryiIDNQNFNSTQLLKEANKNLintk 701
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKEleELEEELEQLRKELEELSRQ-----ISALRKDLARLEAEVEQLE---- 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  702 inyDDLTNLLIDLrngSNYLEEFEGVLWRLNIeykdkfvkrAHDHAMELMRESIRLESLFNKTRDVAVGPLQAAQAYQRI 781
Cdd:TIGR02168  747 ---ERIAQLSKEL---TELEAEIEELEERLEE---------AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  782 VDALlsAEEAAKNASLAAETAFKVAypgDPDKSLVRRATQSLRKSEELhskgEELKMTVGQQFSELDKQRSALGTAKGIL 861
Cdd:TIGR02168  812 LTLL--NEEAANLRERLESLERRIA---ATERRLEDLEEQIEELSEDI----ESLAAEIEELEELIEELESELEALLNER 882
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  862 GVTDDRINGLSTLMETQlstsiSTDIQEVLDRTEETYSNVQKTLDHINAIHMNLTIIReralelSRIDasllyEIRETIS 941
Cdd:TIGR02168  883 ASLEEALALLRSELEEL-----SEELRELESKRSELRRELEELREKLAQLELRLEGLE------VRID-----NLQERLS 946
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 2068726809  942 TGESHTMKGIRKANNLrktgdrIENYSNDLRERIEALKRKIKQ 984
Cdd:TIGR02168  947 EEYSLTLEEAEALENK------IEDDEEEARRRLKRLENKIKE 983
 
Name Accession Description Interval E-value
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1808-1963 2.26e-34

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 129.85  E-value: 2.26e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1808 GSYFPGDAYAIYSDDFNVGSLLELRLEFRTWELNGIILSVADPRGTS-LSLELVNGAVLLTVDMGSGhpfsaRVRLRNKF 1886
Cdd:cd00110      1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDfLALELEDGRLVLRYDLGSG-----SLVLSSKT 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068726809 1887 NFCDNMWHTVKASYIKDSLSLRVDDYREAYGFNGSGNDERTLTGaPFYIGGLPDAALQGTLTARDNFKGCIRNIVLN 1963
Cdd:cd00110     76 PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDG-PLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
Laminin_B pfam00052
Laminin B (Domain IV);
107-244 1.26e-31

Laminin B (Domain IV);


Pssm-ID: 459652  Cd Length: 136  Bit Score: 121.22  E-value: 1.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  107 YWQLPRGFKRDKVTSYNGYLRFRVHSEGGNkifPDQILQSYPLVSLQGNwQLVLEYY-----PPAISTDGRYEVKLHEDY 181
Cdd:pfam00052    1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLP---GGGSLNSEPDVILEGN-GLRLSYSspdqpPPDPGQEQTYSVRLHEEN 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068726809  182 WRLKNKPQkVTREMMMIALQNIQHILIRATHAADATTASIHDVTLDVAAEGSpvSSRVALGVE 244
Cdd:pfam00052   77 WRDSDGAP-VSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGG--SGPPASWVE 136
LamG smart00282
Laminin G domain;
1830-1965 1.32e-28

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 112.43  E-value: 1.32e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  1830 ELRLEFRTWELNGIILSVADPRGTS-LSLELVNGAVLLTVDMGSGhpfsaRVRLRNKFN-FCDNMWHTVKASYIKDSLSL 1907
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDyLALELRDGRLVLRYDLGSG-----PARLTSDPTpLNDGQWHRVAVERNGRSVTL 75
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 2068726809  1908 RVDDYREAYGFNGSGNDERTLTGaPFYIGGLPDAALQGTLTARDNFKGCIRNIVLNSE 1965
Cdd:smart00282   76 SVDGGNRVSGESPGGLTILNLDG-PLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1835-1965 2.29e-28

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 111.36  E-value: 2.29e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1835 FRTWELNGIILSVADPRGTSLSLELVNGAVLLTVDMGSGHPfsarVRLRNKFNFCDNMWHTVKASYIKDSLSLRVDDYRe 1914
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPE----SLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQT- 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2068726809 1915 AYGFNGSGNDERTLTGAPFYIGGLPDAALQGTLTARDNFKGCIRNIVLNSE 1965
Cdd:pfam02210   76 VVSSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1388-1570 2.81e-27

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 109.43  E-value: 2.81e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1388 AGFLGQGFVELP-SHILKRDSNFGFTFQTMEADALLMlstFIGQDNETDgdmstttttttttstptprqpgeehppdYYS 1466
Cdd:cd00110      2 VSFSGSSYVRLPtLPAPRTRLSISFSFRTTSPNGLLL---YAGSQNGGD----------------------------FLA 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1467 VSLVEGHLDIRLNGGTSSHRIMSSAKYNDGYLHSFFVIKENRRVTLKVDDKEVNGTRLDRGSQvvSGPDTGGLYFGGVPR 1546
Cdd:cd00110     51 LELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSA--LLNLDGPLYLGGLPE 128
                          170       180
                   ....*....|....*....|....
gi 2068726809 1547 DIEaVTMVGSSRSLKGCIRDVIIN 1570
Cdd:cd00110    129 DLK-SPGLPVSPGFVGCIRDLKVN 151
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1631-1780 2.23e-23

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 98.26  E-value: 2.23e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1631 ESYVMVPlNSRTFKKNFTVSFEFRTYYPNGLFFivSNTRKKRTQTISAQLRNGRVIVSMEKeskkGPKNIEAASKPGLNT 1710
Cdd:cd00110      7 SSYVRLP-TLPAPRTRLSISFSFRTTSPNGLLL--YAGSQNGGDFLALELEDGRLVLRYDL----GSGSLVLSSKTPLND 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068726809 1711 GQWRKVMIEKFRKRLLLFIDNQLVKKEKAPRK---MNVGRELFLGSLPASDDNPDnMQETETLRGCLRNLKIN 1780
Cdd:cd00110     80 GQWHSVSVERNGRSVTLSVDGERVVESGSPGGsalLNLDGPLYLGGLPEDLKSPG-LPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1648-1782 5.82e-23

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 96.25  E-value: 5.82e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  1648 TVSFEFRTYYPNGLFFivSNTRKKRTQTISAQLRNGRVIVSMEKESkkGPKNIEAASKPgLNTGQWRKVMIEKFRKRLLL 1727
Cdd:smart00282    1 SISFSFRTTSPNGLLL--YAGSKGGGDYLALELRDGRLVLRYDLGS--GPARLTSDPTP-LNDGQWHRVAVERNGRSVTL 75
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 2068726809  1728 FIDNQLVKKEKAPRK---MNVGRELFLGSLPAsDDNPDNMQETETLRGCLRNLKINGE 1782
Cdd:smart00282   76 SVDGGNRVSGESPGGltiLNLDGPLYLGGLPE-DLKLPPLPVTPGFRGCIRNLKVNGK 132
LamB smart00281
Laminin B domain;
105-229 5.08e-22

Laminin B domain;


Pssm-ID: 214597  Cd Length: 127  Bit Score: 93.48  E-value: 5.08e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809   105 PLYWQLPRGFKRDKVTSYNGYLRFRVHSEGGnkifPDQILQSYPLVSLQGNwQLVLEYY---PPAISTDGRYEVKLHEDY 181
Cdd:smart00281    4 PVYWVAPEQFLGDKVTSYGGKLRYTLSFDGR----RGGTHVSAPDVILEGN-GLRISHPaegPPLPDELTTVEVRFREEN 78
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 2068726809   182 WRLKNKpQKVTREMMMIALQNIQHILIRATHAADATTASIHDVTLDVA 229
Cdd:smart00281   79 WQYYGG-RPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVA 125
Laminin_G_1 pfam00054
Laminin G domain;
1457-1572 9.60e-21

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 90.07  E-value: 9.60e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1457 GEEHPPDYYSVSLVEGHLDIRLNGGTSSHRIMSSAKYNDGYLHSFFVIKENRRVTLKVDDKEVNGTRldrgsqVVSGPDT 1536
Cdd:pfam00054   14 GTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE------SPLGATT 87
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2068726809 1537 -----GGLYFGGVPRDIEAVTMVGSSRSLKGCIRDVIINNK 1572
Cdd:pfam00054   88 dldvdGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGK 128
Laminin_G_1 pfam00054
Laminin G domain;
1029-1168 2.21e-20

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 88.91  E-value: 2.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1029 SERNALLVYLGTNNSSDYMAVEMVNRRIEFSWDAGGGAQRITHPLRLltstpyvnDDIRWYYISINRIGNIGQLSVtpan 1108
Cdd:pfam00054    4 TEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKL--------NDGKWHSVELERNGRSGTLSV---- 71
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068726809 1109 veeTGDEVGTIVSNASPAGFSKMDILpsdsLWVGGAPSNVSDLLKTN---KFSGCLHTLSIDG 1168
Cdd:pfam00054   72 ---DGEARPTGESPLGATTDLDVDGP----LYVGGLPSLGVKKRRLAispSFDGCIRDVIVNG 127
LamG smart00282
Laminin G domain;
1030-1169 2.50e-19

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 85.85  E-value: 2.50e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  1030 ERNALLVYLGTNNSSDYMAVEMVNRRIEFSWDAGGGAQRIthplrllTSTPYVNDDIRWYYISINRIGNIGQLSVtpaNV 1109
Cdd:smart00282   10 SPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARL-------TSDPTPLNDGQWHRVAVERNGRSVTLSV---DG 79
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068726809  1110 EETgdevgtiVSNASPAGFSKMDilPSDSLWVGGAPSN--VSDLLKTNKFSGCLHTLSIDGE 1169
Cdd:smart00282   80 GNR-------VSGESPGGLTILN--LDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
LamG smart00282
Laminin G domain;
1408-1572 1.03e-18

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 84.31  E-value: 1.03e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  1408 NFGFTFQTMEADALLMlstFIGQDNETDgdmstttttttttstptprqpgeehppdYYSVSLVEGHLDIRLNGGTSSHRI 1487
Cdd:smart00282    1 SISFSFRTTSPNGLLL---YAGSKGGGD----------------------------YLALELRDGRLVLRYDLGSGPARL 49
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  1488 MSSA-KYNDGYLHSFFVIKENRRVTLKVDDKEVNGTRLDRGSQVVSGPdtGGLYFGGVPRDIEAvTMVGSSRSLKGCIRD 1566
Cdd:smart00282   50 TSDPtPLNDGQWHRVAVERNGRSVTLSVDGGNRVSGESPGGLTILNLD--GPLYLGGLPEDLKL-PPLPVTPGFRGCIRN 126

                    ....*.
gi 2068726809  1567 VIINNK 1572
Cdd:smart00282  127 LKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1007-1167 6.57e-18

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 82.47  E-value: 6.57e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1007 KYRPALQPSTTTNIMLSYgITNSErNALLVYLGTNNSSDYMAVEMVNRRIEFSWDAGGGAQRIthplrllTSTPYVNDDi 1086
Cdd:cd00110     11 RLPTLPAPRTRLSISFSF-RTTSP-NGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVL-------SSKTPLNDG- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1087 RWYYISINRIGNIGQLSVtpanveetgDEvGTIVSNASPAGFSKMDilPSDSLWVGGAP--SNVSDLLKTNKFSGCLHTL 1164
Cdd:cd00110     81 QWHSVSVERNGRSVTLSV---------DG-ERVVESGSPGGSALLN--LDGPLYLGGLPedLKSPGLPVSPGFVGCIRDL 148

                   ...
gi 2068726809 1165 SID 1167
Cdd:cd00110    149 KVN 151
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1653-1782 2.70e-17

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 79.77  E-value: 2.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1653 FRTYYPNGLFFIVSNtrkKRTQTISAQLRNGRVIVSMEKESkkGPKNIEAASKPgLNTGQWRKVMIEKFRKRLLLFIDNQ 1732
Cdd:pfam02210    1 FRTRQPNGLLLYAGG---GGSDFLALELVNGRLVLRYDLGS--GPESLLSSGKN-LNDGQWHSVRVERNGNTLTLSVDGQ 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2068726809 1733 LVKKEKAPRK---MNVGRELFLGSLPASDDNPdNMQETETLRGCLRNLKINGE 1782
Cdd:pfam02210   75 TVVSSLPPGEsllLNLNGPLYLGGLPPLLLLP-ALPVRAGFVGCIRDVRVNGE 126
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
457-700 2.32e-16

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 80.92  E-value: 2.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  457 SINVTAyvpAPWPTIRELQNVTRILRYQLDRYHSNVDvSQELVVEFdLDYYSKDLKQRAEQLEAAARETYPPTAKLRLEA 536
Cdd:pfam06008    3 SLNSLT---GALPAPYKINYNLENLTKQLQEYLSPEN-AHKIQIEI-LEKELSSLAQETEELQKKATQTLAKAQQVNAES 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  537 QSILDILNGLYTQID----------ETIAYLkNYAIGETPSISIGGAMMEAEKILKEIQKRNFTKNDAEAKIELSKAHIL 606
Cdd:pfam06008   78 ERTLGHAKELAEAIKnlidnikeinEKVATL-GENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  607 LKRIMKMDQEH-----PLIEAGRTHIRDIENKLKELLQRIEAANRKTNEASELNKNNAKRLARVQTYSAEiknsryiIDN 681
Cdd:pfam06008  157 LSRIQTWFQSPqeenkALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEE-------VSE 229
                          250
                   ....*....|....*....
gi 2068726809  682 QNFNSTQLLKEANKNLINT 700
Cdd:pfam06008  230 QKNQLEETLKTARDSLDAA 248
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
288-337 1.27e-13

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 66.61  E-value: 1.27e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2068726809  288 CRCNGR---SETCDAETGVCEnCRDHTMGDHCEVCATGYYGNPArerCKPCAC 337
Cdd:pfam00053    1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS---DPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
389-434 4.51e-13

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 65.07  E-value: 4.51e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2068726809  389 PCDCDPFGSVHEGCDR-DGVCTCKPGITGRDCSQCASRHV---TSATGCR 434
Cdd:cd00055      1 PCDCNGHGSLSGQCDPgTGQCECKPNTTGRRCDRCAPGYYglpSQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
288-333 5.70e-13

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 65.07  E-value: 5.70e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2068726809  288 CRCNGR---SETCDAETGVCEnCRDHTMGDHCEVCATGYYGNPAR-ERCK 333
Cdd:cd00055      2 CDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1228-1363 6.35e-13

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 67.44  E-value: 6.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1228 FKTLDEDALLFLAVNEaKNQYFSISLDSGHVVFTVQFDPQTRLLMKSSKQLNNNED-MVQIqaivpnkERGGaRMGRLVV 1306
Cdd:pfam02210    1 FRTRQPNGLLLYAGGG-GSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWhSVRV-------ERNG-NTLTLSV 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2068726809 1307 GDQDQIGTVKGGPDLDL-SFVPYYFGGVDPEFnrgRWGSELVLRSLLGCMTGLSVLDE 1363
Cdd:pfam02210   72 DGQTVVSSLPPGESLLLnLNGPLYLGGLPPLL---LLPALPVRAGFVGCIRDVRVNGE 126
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
390-433 1.09e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 63.87  E-value: 1.09e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2068726809   390 CDCDPFGSVHEGCDRD-GVCTCKPGITGRDCSQCASRHV-TSATGC 433
Cdd:smart00180    1 CDCDPGGSASGTCDPDtGQCECKPNVTGRRCDRCAPGYYgDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
390-433 6.46e-12

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 61.99  E-value: 6.46e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2068726809  390 CDCDPFGSVHEGCDR-DGVCTCKPGITGRDCSQCASRHV----TSATGC 433
Cdd:pfam00053    1 CDCNPHGSLSDTCDPeTGQCLCKPGVTGRHCDRCKPGYYglpsDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
288-328 1.63e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 60.79  E-value: 1.63e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 2068726809   288 CRCNGR---SETCDAETGVCEnCRDHTMGDHCEVCATGYYGNPA 328
Cdd:smart00180    1 CDCDPGgsaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGP 43
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
334-388 1.03e-09

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 55.82  E-value: 1.03e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2068726809  334 PCACPSleqNFAETCQADRYAGyICHCRTGYTGAKCNRCDHGYYGRPSQPRGyCR 388
Cdd:cd00055      1 PCDCNG---HGSLSGQCDPGTG-QCECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
335-387 1.33e-09

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 55.44  E-value: 1.33e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2068726809  335 CACPSLeQNFAETCqaDRYAGYiCHCRTGYTGAKCNRCDHGYYGRPSQPRGYC 387
Cdd:pfam00053    1 CDCNPH-GSLSDTC--DPETGQ-CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1200-1360 1.49e-09

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 58.58  E-value: 1.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1200 AVGFNGKGYFkgknRVRRPKEYYSTV---LAFKTLDEDALLFLAVNEAKNQYFSISLDSGHVVFTVQFDPqTRLLMKSSK 1276
Cdd:cd00110      1 GVSFSGSSYV----RLPTLPAPRTRLsisFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGS-GSLVLSSKT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1277 QLNNNED-MVQIqaivpnkERGGaRMGRLVVGDQDQIGTVKGGPDLDLSFV-PYYFGGVDPEFNRGRwgsELVLRSLLGC 1354
Cdd:cd00110     76 PLNDGQWhSVSV-------ERNG-RSVTLSVDGERVVESGSPGGSALLNLDgPLYLGGLPEDLKSPG---LPVSPGFVGC 144

                   ....*.
gi 2068726809 1355 MTGLSV 1360
Cdd:cd00110    145 IRDLKV 150
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
335-380 3.49e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 51.16  E-value: 3.49e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2068726809   335 CACPsLEQNFAETCqaDRYAGyICHCRTGYTGAKCNRCDHGYYGRP 380
Cdd:smart00180    1 CDCD-PGGSASGTC--DPDTG-QCECKPNVTGRRCDRCAPGYYGDG 42
LamG smart00282
Laminin G domain;
1228-1360 1.14e-07

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 52.34  E-value: 1.14e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  1228 FKTLDEDALLFLAVNEAKNQYFSISLDSGHVVFTVQFDPQTRLLMKSSKQLNNNED-MVQIqaivpnkERGGaRMGRLVV 1306
Cdd:smart00282    6 FRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWhRVAV-------ERNG-RSVTLSV 77
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2068726809  1307 GDQD-QIGTVKGGPDLDLSFVPYYFGGVDPEFNRGRwgsELVLRSLLGCMTGLSV 1360
Cdd:smart00282   78 DGGNrVSGESPGGLTILNLDGPLYLGGLPEDLKLPP---LPVTPGFRGCIRNLKV 129
Laminin_II pfam06009
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ...
895-1019 1.08e-05

Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 368703 [Multi-domain]  Cd Length: 138  Bit Score: 47.10  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  895 EETYSNVQKTLDHINAIHMNLTIIRERaleLSRIDASLlyeirETISTGESHTMKGIRKAN----NLRKTGDRI------ 964
Cdd:pfam06009    6 REANETAKEVLEQLAPLSQNLENTSEK---LSGINRSL-----EETNELVNDANKALDDAGrsvkKLEELAPDLldklkp 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2068726809  965 ----ENYSNDLRERIEALKRKIKQTRQYASSIRVSLttNSSGICTRKYRPalqPSTTTN 1019
Cdd:pfam06009   78 lkqlEVNSSSLSDNISRIKELIAQARKAANSIKVSV--SFDGDSIVELRP---PISVTD 131
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
509-984 1.79e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  509 KDLKQRAEQLEAAARETypptAKLRLEAQSILDILNGLYTQIDETIAYLKNYA--IGETPSISigGAMMEAEKILKEiqK 586
Cdd:PRK03918   231 KELEELKEEIEELEKEL----ESLEGSKRKLEEKIRELEERIEELKKEIEELEekVKELKELK--EKAEEYIKLSEF--Y 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  587 RNFTKNDAEAKIELSKAHILLKRIMKMDQEhplIEAGRTHIRDIENKLKEL---LQRIEAANRKTNEASELnKNNAKRL- 662
Cdd:PRK03918   303 EEYLDELREIEKRLSRLEEEINGIEERIKE---LEEKEERLEELKKKLKELekrLEELEERHELYEEAKAK-KEELERLk 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  663 ARVQTYSAE-IKNSryiIDNQNFNSTQLLKEANKnlINTKINydDLTNLLIDLRNGSNYLEEFEGVL----------WRL 731
Cdd:PRK03918   379 KRLTGLTPEkLEKE---LEELEKAKEEIEEEISK--ITARIG--ELKKEIKELKKAIEELKKAKGKCpvcgrelteeHRK 451
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  732 NI--EYK------DKFVKRAHDHAMELMRESIRLESLFNKTRDVAvgplqaaqAYQRIVDALLSAEEAAKNASL-----A 798
Cdd:PRK03918   452 ELleEYTaelkriEKELKEIEEKERKLRKELRELEKVLKKESELI--------KLKELAEQLKELEEKLKKYNLeelekK 523
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  799 AETAFKVAYPGDPDKSLVRRATQSLRKSEELHSKGEELKMTVGqqfsELDKQRSALGTAKGILGVT-----DDRINGLST 873
Cdd:PRK03918   524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD----ELEEELAELLKELEELGFEsveelEERLKELEP 599
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  874 LMETQLS-TSISTDIQEVLDRTEETYSNVQKTLDHINAIHMNLTIIRERALELSRIDASLLYEIRETISTGESHTMKGIR 952
Cdd:PRK03918   600 FYNEYLElKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLR 679
                          490       500       510
                   ....*....|....*....|....*....|...
gi 2068726809  953 KA-NNLRKTGDRIENYSNDLRERIEALKRKIKQ 984
Cdd:PRK03918   680 AElEELEKRREEIKKTLEKLKEELEEREKAKKE 712
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
474-993 2.70e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 2.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  474 LQNVTRILRYQLDRYHSNVDVSQ---ELVVEF---DLDYYSKDLKQRAEQLEAAAREtypptaklRLEAQSILDILNGLY 547
Cdd:TIGR02168  191 LEDILNELERQLKSLERQAEKAErykELKAELrelELALLVLRLEELREELEELQEE--------LKEAEEELEELTAEL 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  548 TQIDETIAYLKnyaigetpsisigGAMMEAEKILKEIQKRNFTKNDAEAKIELSKAHIllKRimKMDQEHPLIEAGRTHI 627
Cdd:TIGR02168  263 QELEEKLEELR-------------LEVSELEEEIEELQKELYALANEISRLEQQKQIL--RE--RLANLERQLEELEAQL 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  628 RDIENKLKELLqriEAANRKTNEASELNKNNAKRLARVQTYSAEIKNSRYIIDN-----QNFNSTQLLKEANKNLINTKI 702
Cdd:TIGR02168  326 EELESKLDELA---EELAELEEKLEELKEELESLEAELEELEAELEELESRLEEleeqlETLRSKVAQLELQIASLNNEI 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  703 NY---------DDLTNLLIDLRNGSNYLEEFEGVLWRLNIEYKDKFVKRAHDHAMELMRESIRLESLFNKTR---DVAVG 770
Cdd:TIGR02168  403 ERlearlerleDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEqalDAAER 482
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  771 PLQAAQA----YQRIVDALLSAEEAAKNASLAA--------------------ETAFKVAYPGD------PDKSLVRRAT 820
Cdd:TIGR02168  483 ELAQLQArldsLERLQENLEGFSEGVKALLKNQsglsgilgvlselisvdegyEAAIEAALGGRlqavvvENLNAAKKAI 562
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  821 QSLRKSEELHSKGEELKMTVGQQFSELDkqRSALGTAKGILGVTDDRI---NGLSTLMETQLSTS-ISTDIQEVLD---R 893
Cdd:TIGR02168  563 AFLKQNELGRVTFLPLDSIKGTEIQGND--REILKNIEGFLGVAKDLVkfdPKLRKALSYLLGGVlVVDDLDNALElakK 640
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  894 TEETYSNVQKTLDHINAIHM---------NLTIIRERALElsridasllyEIRETISTGESHTMKGIRKANNLRKTGDRI 964
Cdd:TIGR02168  641 LRPGYRIVTLDGDLVRPGGVitggsaktnSSILERRREIE----------ELEEKIEELEEKIAELEKALAELRKELEEL 710
                          570       580
                   ....*....|....*....|....*....
gi 2068726809  965 ENYSNDLRERIEALKRKIKQTRQYASSIR 993
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLE 739
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
624-984 3.63e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 3.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  624 RTHIRDIENKLKELLQRIEAANRKTNEASEL--NKNNAKRLARVQTYSAEIKnsryiIDNQNFNSTQLLKEANKNLintk 701
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKEleELEEELEQLRKELEELSRQ-----ISALRKDLARLEAEVEQLE---- 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  702 inyDDLTNLLIDLrngSNYLEEFEGVLWRLNIeykdkfvkrAHDHAMELMRESIRLESLFNKTRDVAVGPLQAAQAYQRI 781
Cdd:TIGR02168  747 ---ERIAQLSKEL---TELEAEIEELEERLEE---------AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  782 VDALlsAEEAAKNASLAAETAFKVAypgDPDKSLVRRATQSLRKSEELhskgEELKMTVGQQFSELDKQRSALGTAKGIL 861
Cdd:TIGR02168  812 LTLL--NEEAANLRERLESLERRIA---ATERRLEDLEEQIEELSEDI----ESLAAEIEELEELIEELESELEALLNER 882
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  862 GVTDDRINGLSTLMETQlstsiSTDIQEVLDRTEETYSNVQKTLDHINAIHMNLTIIReralelSRIDasllyEIRETIS 941
Cdd:TIGR02168  883 ASLEEALALLRSELEEL-----SEELRELESKRSELRRELEELREKLAQLELRLEGLE------VRID-----NLQERLS 946
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 2068726809  942 TGESHTMKGIRKANNLrktgdrIENYSNDLRERIEALKRKIKQ 984
Cdd:TIGR02168  947 EEYSLTLEEAEALENK------IEDDEEEARRRLKRLENKIKE 983
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
505-703 3.64e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 45.33  E-value: 3.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  505 DYYSKDLKQRAEQLEAAARETYPPTAKLRLEAQSILDILNGLYTQIDETIA---------YLKNYAIGETPSISIGGAMM 575
Cdd:COG5185    253 DKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKsidikkateSLEEQLAAAEAEQELEESKR 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  576 EAEK-ILKEIQKRNFTKNDAEAKIELSKAHI--------LLKRIMKMDQEHPLIEAGRTHI----RDIENKLKELLQ--- 639
Cdd:COG5185    333 ETETgIQNLTAEIEQGQESLTENLEAIKEEIenivgeveLSKSSEELDSFKDTIESTKESLdeipQNQRGYAQEILAtle 412
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068726809  640 ---------------RIEAANRKTNEASELNKNNAKRLARVQTYSAEIKNSRYIIDNQNFNSTQLLKEANKNLINTKIN 703
Cdd:COG5185    413 dtlkaadrqieelqrQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIE 491
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
576-716 2.58e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.70  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  576 EAEKILKEIQKRNFTKNDAEAKIELSKAHILLKRIMKMDQEHPLIEAGRTHIRDIENKLKellqrieaaNRKTNEASELN 655
Cdd:TIGR04523  172 ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLK---------DNIEKKQQEIN 242
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068726809  656 KNNAKrLARVQTYSAEIKNSRYIIDNQNFNSTQLLKEANKNLINTKINYDDLTNLLIDLRN 716
Cdd:TIGR04523  243 EKTTE-ISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN 302
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
547-751 7.43e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 41.74  E-value: 7.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  547 YTQIDETIAYLKN-YAIGETPSI-----SIGGAMMEAE----KILKEIQKRNFTKNDAEAKIELSKAHIllKRIM----- 611
Cdd:PTZ00440  1274 NNKMENALHEIKNmYEFLISIDSekilkEILNSTKKAEefsnDAKKELEKTDNLIKQVEAKIEQAKEHK--NKIYgsled 1351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  612 -KMDQEHPLIEAGRTHIRDIENKLKELLQRIEAANrktnEASELNKNNAKRlarvQTYSAEIKNSRYII---DNQNFN-- 685
Cdd:PTZ00440  1352 kQIDDEIKKIEQIKEEISNKRKEINKYLSNIKSNK----EKCDLHVRNASR----GKDKIDFLNKHEAIepsNSKEVNii 1423
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068726809  686 --------STQLLKEANKNLINTKINYDDLTNLLIDLRNGSNYLEefegvlwRLNIEYKDKFVKRAHDHAMELM 751
Cdd:PTZ00440  1424 kitdninkCKQYSNEAMETENKADENNDSIIKYEKEITNILNNSS-------ILGKKTKLEKKKKEATNIMDDI 1490
 
Name Accession Description Interval E-value
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1808-1963 2.26e-34

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 129.85  E-value: 2.26e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1808 GSYFPGDAYAIYSDDFNVGSLLELRLEFRTWELNGIILSVADPRGTS-LSLELVNGAVLLTVDMGSGhpfsaRVRLRNKF 1886
Cdd:cd00110      1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDfLALELEDGRLVLRYDLGSG-----SLVLSSKT 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068726809 1887 NFCDNMWHTVKASYIKDSLSLRVDDYREAYGFNGSGNDERTLTGaPFYIGGLPDAALQGTLTARDNFKGCIRNIVLN 1963
Cdd:cd00110     76 PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDG-PLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
Laminin_B pfam00052
Laminin B (Domain IV);
107-244 1.26e-31

Laminin B (Domain IV);


Pssm-ID: 459652  Cd Length: 136  Bit Score: 121.22  E-value: 1.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  107 YWQLPRGFKRDKVTSYNGYLRFRVHSEGGNkifPDQILQSYPLVSLQGNwQLVLEYY-----PPAISTDGRYEVKLHEDY 181
Cdd:pfam00052    1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLP---GGGSLNSEPDVILEGN-GLRLSYSspdqpPPDPGQEQTYSVRLHEEN 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068726809  182 WRLKNKPQkVTREMMMIALQNIQHILIRATHAADATTASIHDVTLDVAAEGSpvSSRVALGVE 244
Cdd:pfam00052   77 WRDSDGAP-VSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGG--SGPPASWVE 136
LamG smart00282
Laminin G domain;
1830-1965 1.32e-28

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 112.43  E-value: 1.32e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  1830 ELRLEFRTWELNGIILSVADPRGTS-LSLELVNGAVLLTVDMGSGhpfsaRVRLRNKFN-FCDNMWHTVKASYIKDSLSL 1907
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGDyLALELRDGRLVLRYDLGSG-----PARLTSDPTpLNDGQWHRVAVERNGRSVTL 75
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 2068726809  1908 RVDDYREAYGFNGSGNDERTLTGaPFYIGGLPDAALQGTLTARDNFKGCIRNIVLNSE 1965
Cdd:smart00282   76 SVDGGNRVSGESPGGLTILNLDG-PLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1835-1965 2.29e-28

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 111.36  E-value: 2.29e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1835 FRTWELNGIILSVADPRGTSLSLELVNGAVLLTVDMGSGHPfsarVRLRNKFNFCDNMWHTVKASYIKDSLSLRVDDYRe 1914
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPE----SLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQT- 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2068726809 1915 AYGFNGSGNDERTLTGAPFYIGGLPDAALQGTLTARDNFKGCIRNIVLNSE 1965
Cdd:pfam02210   76 VVSSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1388-1570 2.81e-27

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 109.43  E-value: 2.81e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1388 AGFLGQGFVELP-SHILKRDSNFGFTFQTMEADALLMlstFIGQDNETDgdmstttttttttstptprqpgeehppdYYS 1466
Cdd:cd00110      2 VSFSGSSYVRLPtLPAPRTRLSISFSFRTTSPNGLLL---YAGSQNGGD----------------------------FLA 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1467 VSLVEGHLDIRLNGGTSSHRIMSSAKYNDGYLHSFFVIKENRRVTLKVDDKEVNGTRLDRGSQvvSGPDTGGLYFGGVPR 1546
Cdd:cd00110     51 LELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSA--LLNLDGPLYLGGLPE 128
                          170       180
                   ....*....|....*....|....
gi 2068726809 1547 DIEaVTMVGSSRSLKGCIRDVIIN 1570
Cdd:cd00110    129 DLK-SPGLPVSPGFVGCIRDLKVN 151
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1631-1780 2.23e-23

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 98.26  E-value: 2.23e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1631 ESYVMVPlNSRTFKKNFTVSFEFRTYYPNGLFFivSNTRKKRTQTISAQLRNGRVIVSMEKeskkGPKNIEAASKPGLNT 1710
Cdd:cd00110      7 SSYVRLP-TLPAPRTRLSISFSFRTTSPNGLLL--YAGSQNGGDFLALELEDGRLVLRYDL----GSGSLVLSSKTPLND 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068726809 1711 GQWRKVMIEKFRKRLLLFIDNQLVKKEKAPRK---MNVGRELFLGSLPASDDNPDnMQETETLRGCLRNLKIN 1780
Cdd:cd00110     80 GQWHSVSVERNGRSVTLSVDGERVVESGSPGGsalLNLDGPLYLGGLPEDLKSPG-LPVSPGFVGCIRDLKVN 151
LamG smart00282
Laminin G domain;
1648-1782 5.82e-23

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 96.25  E-value: 5.82e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  1648 TVSFEFRTYYPNGLFFivSNTRKKRTQTISAQLRNGRVIVSMEKESkkGPKNIEAASKPgLNTGQWRKVMIEKFRKRLLL 1727
Cdd:smart00282    1 SISFSFRTTSPNGLLL--YAGSKGGGDYLALELRDGRLVLRYDLGS--GPARLTSDPTP-LNDGQWHRVAVERNGRSVTL 75
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 2068726809  1728 FIDNQLVKKEKAPRK---MNVGRELFLGSLPAsDDNPDNMQETETLRGCLRNLKINGE 1782
Cdd:smart00282   76 SVDGGNRVSGESPGGltiLNLDGPLYLGGLPE-DLKLPPLPVTPGFRGCIRNLKVNGK 132
Laminin_G_1 pfam00054
Laminin G domain;
1835-1964 1.06e-22

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 95.46  E-value: 1.06e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1835 FRTWELNGIILSVA-DPRGTSLSLELVNGAVLLTVDMGSGhpfsaRVRLRNKFNFCDNMWHTVKASYIKDSLSLRVDDYR 1913
Cdd:pfam00054    1 FRTTEPSGLLLYNGtQTERDFLALELRDGRLEVSYDLGSG-----AAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEA 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2068726809 1914 EAYGFNGSGNDERTLTGAPFYIGGLPDAALQGTLTA-RDNFKGCIRNIVLNS 1964
Cdd:pfam00054   76 RPTGESPLGATTDLDVDGPLYVGGLPSLGVKKRRLAiSPSFDGCIRDVIVNG 127
LamB smart00281
Laminin B domain;
105-229 5.08e-22

Laminin B domain;


Pssm-ID: 214597  Cd Length: 127  Bit Score: 93.48  E-value: 5.08e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809   105 PLYWQLPRGFKRDKVTSYNGYLRFRVHSEGGnkifPDQILQSYPLVSLQGNwQLVLEYY---PPAISTDGRYEVKLHEDY 181
Cdd:smart00281    4 PVYWVAPEQFLGDKVTSYGGKLRYTLSFDGR----RGGTHVSAPDVILEGN-GLRISHPaegPPLPDELTTVEVRFREEN 78
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 2068726809   182 WRLKNKpQKVTREMMMIALQNIQHILIRATHAADATTASIHDVTLDVA 229
Cdd:smart00281   79 WQYYGG-RPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVA 125
Laminin_G_1 pfam00054
Laminin G domain;
1457-1572 9.60e-21

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 90.07  E-value: 9.60e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1457 GEEHPPDYYSVSLVEGHLDIRLNGGTSSHRIMSSAKYNDGYLHSFFVIKENRRVTLKVDDKEVNGTRldrgsqVVSGPDT 1536
Cdd:pfam00054   14 GTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE------SPLGATT 87
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2068726809 1537 -----GGLYFGGVPRDIEAVTMVGSSRSLKGCIRDVIINNK 1572
Cdd:pfam00054   88 dldvdGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGK 128
Laminin_G_1 pfam00054
Laminin G domain;
1029-1168 2.21e-20

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 88.91  E-value: 2.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1029 SERNALLVYLGTNNSSDYMAVEMVNRRIEFSWDAGGGAQRITHPLRLltstpyvnDDIRWYYISINRIGNIGQLSVtpan 1108
Cdd:pfam00054    4 TEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKL--------NDGKWHSVELERNGRSGTLSV---- 71
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068726809 1109 veeTGDEVGTIVSNASPAGFSKMDILpsdsLWVGGAPSNVSDLLKTN---KFSGCLHTLSIDG 1168
Cdd:pfam00054   72 ---DGEARPTGESPLGATTDLDVDGP----LYVGGLPSLGVKKRRLAispSFDGCIRDVIVNG 127
LamG smart00282
Laminin G domain;
1030-1169 2.50e-19

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 85.85  E-value: 2.50e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  1030 ERNALLVYLGTNNSSDYMAVEMVNRRIEFSWDAGGGAQRIthplrllTSTPYVNDDIRWYYISINRIGNIGQLSVtpaNV 1109
Cdd:smart00282   10 SPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARL-------TSDPTPLNDGQWHRVAVERNGRSVTLSV---DG 79
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068726809  1110 EETgdevgtiVSNASPAGFSKMDilPSDSLWVGGAPSN--VSDLLKTNKFSGCLHTLSIDGE 1169
Cdd:smart00282   80 GNR-------VSGESPGGLTILN--LDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
LamG smart00282
Laminin G domain;
1408-1572 1.03e-18

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 84.31  E-value: 1.03e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  1408 NFGFTFQTMEADALLMlstFIGQDNETDgdmstttttttttstptprqpgeehppdYYSVSLVEGHLDIRLNGGTSSHRI 1487
Cdd:smart00282    1 SISFSFRTTSPNGLLL---YAGSKGGGD----------------------------YLALELRDGRLVLRYDLGSGPARL 49
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  1488 MSSA-KYNDGYLHSFFVIKENRRVTLKVDDKEVNGTRLDRGSQVVSGPdtGGLYFGGVPRDIEAvTMVGSSRSLKGCIRD 1566
Cdd:smart00282   50 TSDPtPLNDGQWHRVAVERNGRSVTLSVDGGNRVSGESPGGLTILNLD--GPLYLGGLPEDLKL-PPLPVTPGFRGCIRN 126

                    ....*.
gi 2068726809  1567 VIINNK 1572
Cdd:smart00282  127 LKVNGK 132
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1007-1167 6.57e-18

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 82.47  E-value: 6.57e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1007 KYRPALQPSTTTNIMLSYgITNSErNALLVYLGTNNSSDYMAVEMVNRRIEFSWDAGGGAQRIthplrllTSTPYVNDDi 1086
Cdd:cd00110     11 RLPTLPAPRTRLSISFSF-RTTSP-NGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVL-------SSKTPLNDG- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1087 RWYYISINRIGNIGQLSVtpanveetgDEvGTIVSNASPAGFSKMDilPSDSLWVGGAP--SNVSDLLKTNKFSGCLHTL 1164
Cdd:cd00110     81 QWHSVSVERNGRSVTLSV---------DG-ERVVESGSPGGSALLN--LDGPLYLGGLPedLKSPGLPVSPGFVGCIRDL 148

                   ...
gi 2068726809 1165 SID 1167
Cdd:cd00110    149 KVN 151
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1653-1782 2.70e-17

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 79.77  E-value: 2.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1653 FRTYYPNGLFFIVSNtrkKRTQTISAQLRNGRVIVSMEKESkkGPKNIEAASKPgLNTGQWRKVMIEKFRKRLLLFIDNQ 1732
Cdd:pfam02210    1 FRTRQPNGLLLYAGG---GGSDFLALELVNGRLVLRYDLGS--GPESLLSSGKN-LNDGQWHSVRVERNGNTLTLSVDGQ 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2068726809 1733 LVKKEKAPRK---MNVGRELFLGSLPASDDNPdNMQETETLRGCLRNLKINGE 1782
Cdd:pfam02210   75 TVVSSLPPGEsllLNLNGPLYLGGLPPLLLLP-ALPVRAGFVGCIRDVRVNGE 126
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1460-1572 1.15e-16

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 78.23  E-value: 1.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1460 HPPDYYSVSLVEGHLDIRLNGGTSSHRIMSS-AKYNDGYLHSFFVIKENRRVTLKVDDKEVNGTRLDRGSQVVsgPDTGG 1538
Cdd:pfam02210   16 GGSDFLALELVNGRLVLRYDLGSGPESLLSSgKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPPGESLLL--NLNGP 93
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2068726809 1539 LYFGGVPRDiEAVTMVGSSRSLKGCIRDVIINNK 1572
Cdd:pfam02210   94 LYLGGLPPL-LLLPALPVRAGFVGCIRDVRVNGE 126
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
457-700 2.32e-16

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 80.92  E-value: 2.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  457 SINVTAyvpAPWPTIRELQNVTRILRYQLDRYHSNVDvSQELVVEFdLDYYSKDLKQRAEQLEAAARETYPPTAKLRLEA 536
Cdd:pfam06008    3 SLNSLT---GALPAPYKINYNLENLTKQLQEYLSPEN-AHKIQIEI-LEKELSSLAQETEELQKKATQTLAKAQQVNAES 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  537 QSILDILNGLYTQID----------ETIAYLkNYAIGETPSISIGGAMMEAEKILKEIQKRNFTKNDAEAKIELSKAHIL 606
Cdd:pfam06008   78 ERTLGHAKELAEAIKnlidnikeinEKVATL-GENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  607 LKRIMKMDQEH-----PLIEAGRTHIRDIENKLKELLQRIEAANRKTNEASELNKNNAKRLARVQTYSAEiknsryiIDN 681
Cdd:pfam06008  157 LSRIQTWFQSPqeenkALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEE-------VSE 229
                          250
                   ....*....|....*....
gi 2068726809  682 QNFNSTQLLKEANKNLINT 700
Cdd:pfam06008  230 QKNQLEETLKTARDSLDAA 248
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
288-337 1.27e-13

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 66.61  E-value: 1.27e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2068726809  288 CRCNGR---SETCDAETGVCEnCRDHTMGDHCEVCATGYYGNPArerCKPCAC 337
Cdd:pfam00053    1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS---DPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
389-434 4.51e-13

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 65.07  E-value: 4.51e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2068726809  389 PCDCDPFGSVHEGCDR-DGVCTCKPGITGRDCSQCASRHV---TSATGCR 434
Cdd:cd00055      1 PCDCNGHGSLSGQCDPgTGQCECKPNTTGRRCDRCAPGYYglpSQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
288-333 5.70e-13

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 65.07  E-value: 5.70e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2068726809  288 CRCNGR---SETCDAETGVCEnCRDHTMGDHCEVCATGYYGNPAR-ERCK 333
Cdd:cd00055      2 CDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1228-1363 6.35e-13

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 67.44  E-value: 6.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1228 FKTLDEDALLFLAVNEaKNQYFSISLDSGHVVFTVQFDPQTRLLMKSSKQLNNNED-MVQIqaivpnkERGGaRMGRLVV 1306
Cdd:pfam02210    1 FRTRQPNGLLLYAGGG-GSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWhSVRV-------ERNG-NTLTLSV 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2068726809 1307 GDQDQIGTVKGGPDLDL-SFVPYYFGGVDPEFnrgRWGSELVLRSLLGCMTGLSVLDE 1363
Cdd:pfam02210   72 DGQTVVSSLPPGESLLLnLNGPLYLGGLPPLL---LLPALPVRAGFVGCIRDVRVNGE 126
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
390-433 1.09e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 63.87  E-value: 1.09e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2068726809   390 CDCDPFGSVHEGCDRD-GVCTCKPGITGRDCSQCASRHV-TSATGC 433
Cdd:smart00180    1 CDCDPGGSASGTCDPDtGQCECKPNVTGRRCDRCAPGYYgDGPPGC 46
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1029-1169 3.67e-12

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 65.13  E-value: 3.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1029 SERNALLVYLGtNNSSDYMAVEMVNRRIEFSWDAGGGaqrithPLRLLTSTPYVNDDiRWYYISINRIGNIGQLSVtpan 1108
Cdd:pfam02210    4 RQPNGLLLYAG-GGGSDFLALELVNGRLVLRYDLGSG------PESLLSSGKNLNDG-QWHSVRVERNGNTLTLSV---- 71
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068726809 1109 veetgDEVGTIVSNASPAGFskmDILPSDSLWVGGAPSNVSDLLKTNK--FSGCLHTLSIDGE 1169
Cdd:pfam02210   72 -----DGQTVVSSLPPGESL---LLNLNGPLYLGGLPPLLLLPALPVRagFVGCIRDVRVNGE 126
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
390-433 6.46e-12

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 61.99  E-value: 6.46e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2068726809  390 CDCDPFGSVHEGCDR-DGVCTCKPGITGRDCSQCASRHV----TSATGC 433
Cdd:pfam00053    1 CDCNPHGSLSDTCDPeTGQCLCKPGVTGRHCDRCKPGYYglpsDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
288-328 1.63e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 60.79  E-value: 1.63e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 2068726809   288 CRCNGR---SETCDAETGVCEnCRDHTMGDHCEVCATGYYGNPA 328
Cdd:smart00180    1 CDCDPGgsaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGP 43
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
334-388 1.03e-09

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 55.82  E-value: 1.03e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2068726809  334 PCACPSleqNFAETCQADRYAGyICHCRTGYTGAKCNRCDHGYYGRPSQPRGyCR 388
Cdd:cd00055      1 PCDCNG---HGSLSGQCDPGTG-QCECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
335-387 1.33e-09

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 55.44  E-value: 1.33e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2068726809  335 CACPSLeQNFAETCqaDRYAGYiCHCRTGYTGAKCNRCDHGYYGRPSQPRGYC 387
Cdd:pfam00053    1 CDCNPH-GSLSDTC--DPETGQ-CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1200-1360 1.49e-09

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 58.58  E-value: 1.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1200 AVGFNGKGYFkgknRVRRPKEYYSTV---LAFKTLDEDALLFLAVNEAKNQYFSISLDSGHVVFTVQFDPqTRLLMKSSK 1276
Cdd:cd00110      1 GVSFSGSSYV----RLPTLPAPRTRLsisFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGS-GSLVLSSKT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1277 QLNNNED-MVQIqaivpnkERGGaRMGRLVVGDQDQIGTVKGGPDLDLSFV-PYYFGGVDPEFNRGRwgsELVLRSLLGC 1354
Cdd:cd00110     76 PLNDGQWhSVSV-------ERNG-RSVTLSVDGERVVESGSPGGSALLNLDgPLYLGGLPEDLKSPG---LPVSPGFVGC 144

                   ....*.
gi 2068726809 1355 MTGLSV 1360
Cdd:cd00110    145 IRDLKV 150
Laminin_G_1 pfam00054
Laminin G domain;
1653-1781 2.39e-09

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 57.33  E-value: 2.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809 1653 FRTYYPNGLFFivSNTRKKRTQTISAQLRNGRVIVSMEKESkkGPKNIEaaSKPGLNTGQWRKVMIEKFRKRLLLFIDNQ 1732
Cdd:pfam00054    1 FRTTEPSGLLL--YNGTQTERDFLALELRDGRLEVSYDLGS--GAAVVR--SGDKLNDGKWHSVELERNGRSGTLSVDGE 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2068726809 1733 LVK---KEKAPRKM-NVGRELFLGSLPASDDNPDNMQETETLRGCLRNLKING 1781
Cdd:pfam00054   75 ARPtgeSPLGATTDlDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNG 127
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
335-380 3.49e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 51.16  E-value: 3.49e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2068726809   335 CACPsLEQNFAETCqaDRYAGyICHCRTGYTGAKCNRCDHGYYGRP 380
Cdd:smart00180    1 CDCD-PGGSASGTC--DPDTG-QCECKPNVTGRRCDRCAPGYYGDG 42
LamG smart00282
Laminin G domain;
1228-1360 1.14e-07

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 52.34  E-value: 1.14e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  1228 FKTLDEDALLFLAVNEAKNQYFSISLDSGHVVFTVQFDPQTRLLMKSSKQLNNNED-MVQIqaivpnkERGGaRMGRLVV 1306
Cdd:smart00282    6 FRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWhRVAV-------ERNG-RSVTLSV 77
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 2068726809  1307 GDQD-QIGTVKGGPDLDLSFVPYYFGGVDPEFNRGRwgsELVLRSLLGCMTGLSV 1360
Cdd:smart00282   78 DGGNrVSGESPGGLTILNLDGPLYLGGLPEDLKLPP---LPVTPGFRGCIRNLKV 129
TNFRSF16 cd13416
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ...
295-458 2.47e-07

Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.


Pssm-ID: 276921 [Multi-domain]  Cd Length: 159  Bit Score: 52.30  E-value: 2.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  295 ETCDAETGVCENC-RDHTMgdhCEVCATGYYGNP---ARERCKPCA-CPSLEQNFAeTCQADryagyichcrtgyTGAKC 369
Cdd:cd13416     16 EQCPPGEGVARPCgDNQTV---CEPCLDGVTFSDvvsHTEPCQPCTrCPGLMSMRA-PCTAT-------------HDTVC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  370 nRCDHGYYgrPSQPRGYCRPCD-CDP-FGsVHEGC--DRDGVC-TCKPGI---TGRDCSQCASrhvtsatgCRSCEDGcv 441
Cdd:cd13416     79 -ECAYGYY--LDEDSGTCEPCTvCPPgQG-VVQSCgpNQDTVCeACPEGTysdEDSSTDPCLP--------CTVCEDG-- 144
                          170
                   ....*....|....*..
gi 2068726809  442 nilldevEQMIRAATSI 458
Cdd:cd13416    145 -------EVELRECTPV 154
TNFRSF4 cd13406
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ...
347-426 2.16e-06

Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.


Pssm-ID: 276911 [Multi-domain]  Cd Length: 142  Bit Score: 49.32  E-value: 2.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  347 TCQADRY-AGYIC--HCRTGY---------TGAKCNRCDHGYYgrpSQPRGY--CRPCD-CDPF-GSVHEG-CD--RDGV 407
Cdd:cd13406      2 HCVGDTYpSGEKCchECPPGEgmesrctgtQDTVCSPCEPGFY---NEAVNYepCKPCTqCNQRsGSEEKQkCTktSDTV 78
                           90       100
                   ....*....|....*....|....*.
gi 2068726809  408 CTCKPGIT-------GRDCSQCASRH 426
Cdd:cd13406     79 CRCRPGTQpldsykpGVDCVPCPPGH 104
TNFRSF cd00185
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) ...
359-423 1.08e-05

Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) interactions with TNF superfamily (TNFSF) ligands (TNFL) control key cellular processes such as differentiation, proliferation, apoptosis, and cell growth. Dysregulation of these pathways has been shown to result in a wide range of pathological conditions, including autoimmune diseases, inflammation, cancer, and viral infection. There are 29 very diverse family members of TNFRSF reported in humans: 22 are type I transmembrane receptors (single pass with the N terminus on extracellular side of the cell membrane) and have a clear signal peptide; the remaining 7 members are either type III transmembrane receptors (single pass with the N terminus on extracellular side of the membrane but no signal sequence; TNFR13B, TNFR13C, TNFR17, and XEDAR), or attached to the membrane via a glycosylphosphatidylinositol (GPI) linker (TNFR10C), or secreted as soluble receptors (TNFR11B and TNFR6B). All TNFRs contain relatively short cysteine-rich domains (CRDs) in the ectodomain, and are involved in interaction with the TNF homology domain (THD) of their ligands. TNFRs often have multiple CRDs (between one and six), with the most frequent configurations of three or four copies; most CRDs possess three disulfide bridges, but could have between one and four. Localized or genome-wide duplication and evolution of the TNFRSF members appear to have paralleled the emergence of the adaptive immune system; teleosts (i.e. ray-finned, bony fish), which possess an immune system with B and T cells, possess primary and secondary lymphoid organs, and are capable of adaptive responses to pathogens also display several characteristics that are different from the mammalian immune system, making teleost TNFSF orthologs and paralogs of interest to better understand immune system evolution and the immunological pathways elicited to pathogens.


Pssm-ID: 276900 [Multi-domain]  Cd Length: 87  Bit Score: 45.66  E-value: 1.08e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068726809  359 HCrTGYTGAKCNRCDHGYYGRPSQPRGYCRPC-DCDPFGSV-HEGCDR--DGVCTCKPG------ITGRDCSQCA 423
Cdd:cd00185     14 DC-TATTDTVCSPCPPGTYSESWNSLSKCLPCtTCGGGNQVeKTPCTAtdNRCCTCKPGfycdegTNVEECKPCT 87
Laminin_II pfam06009
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ...
895-1019 1.08e-05

Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 368703 [Multi-domain]  Cd Length: 138  Bit Score: 47.10  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  895 EETYSNVQKTLDHINAIHMNLTIIRERaleLSRIDASLlyeirETISTGESHTMKGIRKAN----NLRKTGDRI------ 964
Cdd:pfam06009    6 REANETAKEVLEQLAPLSQNLENTSEK---LSGINRSL-----EETNELVNDANKALDDAGrsvkKLEELAPDLldklkp 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2068726809  965 ----ENYSNDLRERIEALKRKIKQTRQYASSIRVSLttNSSGICTRKYRPalqPSTTTN 1019
Cdd:pfam06009   78 lkqlEVNSSSLSDNISRIKELIAQARKAANSIKVSV--SFDGDSIVELRP---PISVTD 131
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
509-984 1.79e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  509 KDLKQRAEQLEAAARETypptAKLRLEAQSILDILNGLYTQIDETIAYLKNYA--IGETPSISigGAMMEAEKILKEiqK 586
Cdd:PRK03918   231 KELEELKEEIEELEKEL----ESLEGSKRKLEEKIRELEERIEELKKEIEELEekVKELKELK--EKAEEYIKLSEF--Y 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  587 RNFTKNDAEAKIELSKAHILLKRIMKMDQEhplIEAGRTHIRDIENKLKEL---LQRIEAANRKTNEASELnKNNAKRL- 662
Cdd:PRK03918   303 EEYLDELREIEKRLSRLEEEINGIEERIKE---LEEKEERLEELKKKLKELekrLEELEERHELYEEAKAK-KEELERLk 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  663 ARVQTYSAE-IKNSryiIDNQNFNSTQLLKEANKnlINTKINydDLTNLLIDLRNGSNYLEEFEGVL----------WRL 731
Cdd:PRK03918   379 KRLTGLTPEkLEKE---LEELEKAKEEIEEEISK--ITARIG--ELKKEIKELKKAIEELKKAKGKCpvcgrelteeHRK 451
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  732 NI--EYK------DKFVKRAHDHAMELMRESIRLESLFNKTRDVAvgplqaaqAYQRIVDALLSAEEAAKNASL-----A 798
Cdd:PRK03918   452 ELleEYTaelkriEKELKEIEEKERKLRKELRELEKVLKKESELI--------KLKELAEQLKELEEKLKKYNLeelekK 523
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  799 AETAFKVAYPGDPDKSLVRRATQSLRKSEELHSKGEELKMTVGqqfsELDKQRSALGTAKGILGVT-----DDRINGLST 873
Cdd:PRK03918   524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD----ELEEELAELLKELEELGFEsveelEERLKELEP 599
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  874 LMETQLS-TSISTDIQEVLDRTEETYSNVQKTLDHINAIHMNLTIIRERALELSRIDASLLYEIRETISTGESHTMKGIR 952
Cdd:PRK03918   600 FYNEYLElKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLR 679
                          490       500       510
                   ....*....|....*....|....*....|...
gi 2068726809  953 KA-NNLRKTGDRIENYSNDLRERIEALKRKIKQ 984
Cdd:PRK03918   680 AElEELEKRREEIKKTLEKLKEELEEREKAKKE 712
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
474-993 2.70e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 2.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  474 LQNVTRILRYQLDRYHSNVDVSQ---ELVVEF---DLDYYSKDLKQRAEQLEAAAREtypptaklRLEAQSILDILNGLY 547
Cdd:TIGR02168  191 LEDILNELERQLKSLERQAEKAErykELKAELrelELALLVLRLEELREELEELQEE--------LKEAEEELEELTAEL 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  548 TQIDETIAYLKnyaigetpsisigGAMMEAEKILKEIQKRNFTKNDAEAKIELSKAHIllKRimKMDQEHPLIEAGRTHI 627
Cdd:TIGR02168  263 QELEEKLEELR-------------LEVSELEEEIEELQKELYALANEISRLEQQKQIL--RE--RLANLERQLEELEAQL 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  628 RDIENKLKELLqriEAANRKTNEASELNKNNAKRLARVQTYSAEIKNSRYIIDN-----QNFNSTQLLKEANKNLINTKI 702
Cdd:TIGR02168  326 EELESKLDELA---EELAELEEKLEELKEELESLEAELEELEAELEELESRLEEleeqlETLRSKVAQLELQIASLNNEI 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  703 NY---------DDLTNLLIDLRNGSNYLEEFEGVLWRLNIEYKDKFVKRAHDHAMELMRESIRLESLFNKTR---DVAVG 770
Cdd:TIGR02168  403 ERlearlerleDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEqalDAAER 482
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  771 PLQAAQA----YQRIVDALLSAEEAAKNASLAA--------------------ETAFKVAYPGD------PDKSLVRRAT 820
Cdd:TIGR02168  483 ELAQLQArldsLERLQENLEGFSEGVKALLKNQsglsgilgvlselisvdegyEAAIEAALGGRlqavvvENLNAAKKAI 562
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  821 QSLRKSEELHSKGEELKMTVGQQFSELDkqRSALGTAKGILGVTDDRI---NGLSTLMETQLSTS-ISTDIQEVLD---R 893
Cdd:TIGR02168  563 AFLKQNELGRVTFLPLDSIKGTEIQGND--REILKNIEGFLGVAKDLVkfdPKLRKALSYLLGGVlVVDDLDNALElakK 640
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  894 TEETYSNVQKTLDHINAIHM---------NLTIIRERALElsridasllyEIRETISTGESHTMKGIRKANNLRKTGDRI 964
Cdd:TIGR02168  641 LRPGYRIVTLDGDLVRPGGVitggsaktnSSILERRREIE----------ELEEKIEELEEKIAELEKALAELRKELEEL 710
                          570       580
                   ....*....|....*....|....*....
gi 2068726809  965 ENYSNDLRERIEALKRKIKQTRQYASSIR 993
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLE 739
DSL pfam01414
Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain ...
372-421 3.62e-05

Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain defined by structure.


Pssm-ID: 460202  Cd Length: 46  Bit Score: 42.61  E-value: 3.62e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2068726809  372 CDHGYYGrpSQPRGYCRPCDcDPFGsvHEGCDRDGVCTCKPGITGRDCSQ 421
Cdd:pfam01414    1 CDENYYG--STCSKFCRPRD-DKFG--HYTCDANGNKVCLPGWTGPYCDK 45
TNFRSF6_teleost cd13423
Tumor necrosis factor receptor superfamily member 6 (TNFRSF6) in teleosts; also known as fas ...
319-422 7.04e-05

Tumor necrosis factor receptor superfamily member 6 (TNFRSF6) in teleosts; also known as fas cell surface death receptor (FasR); This subfamily of TNFRSF6 (also known as fas cell surface death receptor (FasR) or Fas; APT1; CD95; FAS1; APO-1; FASTM; ALPS1A) is found in teleosts. It contains a death domain and plays a central role in the physiological regulation of programmed cell death. In humans, it has been implicated in the pathogenesis of various malignancies and diseases of the immune system. The receptor interactions with the Fas ligand (FasL), allowing the formation of a death-inducing signaling complex that includes Fas-associated death domain protein (FADD), caspase 8, and caspase 10; autoproteolytic processing of the caspases in the complex triggers a downstream caspase cascade, leading to apoptosis. This receptor has also been shown to activate NF-kappaB, MAPK3/ERK1, and MAPK8/JNK, and is involved in transducing the proliferating signals in normal diploid fibroblast and T cells. In channel catfish and the Japanese rice fish, medaka, homologs of Fas receptor (FasR), as well as FADD and caspase 8, have been identified and characterized, and likely constitute the teleost equivalent of the death-inducing signaling complex (DISC). FasL/FasR are involved in the initiation of apoptosis and suggest that mechanisms of cell-mediated cytotoxicity in teleosts are similar to those used by mammals; presumably, the mechanism of apoptosis induction via death receptors was evolutionarily established during the appearance of vertebrates.


Pssm-ID: 276928 [Multi-domain]  Cd Length: 103  Bit Score: 43.57  E-value: 7.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  319 CATGYYGNPARERCKpcaCPsleqnfaetcqadryAGY--ICHCRTGYTGAKCNRCDHGYYGRPSQPRGYCRPCD-CDPF 395
Cdd:cd13423      2 CEDGTYQHEGLTCCL---CP---------------AGQhvEKHCTNNGTDGECEACEDGTYNSHPNSLDSCEPCTsCDPN 63
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2068726809  396 GS--VHEGCD--RDGVCTCKPGI---TGRDCSQC 422
Cdd:cd13423     64 ANleVEERCTpsSDTVCRCKEGHycdKGEECKVC 97
VSP pfam03302
Giardia variant-specific surface protein;
296-441 1.82e-04

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 46.12  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  296 TCDAeTGVC--ENCRDHTMGDH--CEVCATGYYGNPARErCKPcACPSLEQNFAETCQADRYAGYIC---HCRTGYTGAK 368
Cdd:pfam03302   16 KCTS-SAPCktENCKACSNDKRevCEECNSNNYLTPTSQ-CID-DCAKIGNYYYTTNANNKKICKECtvaNCKTCEDQGQ 92
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068726809  369 CNRCDHGYYgRPSQPrgyCRPCdcdpfgsvHEGCDrdgvcTCKPGiTGRDCSQCAS----RHVTSATGCrSCEDGCV 441
Cdd:pfam03302   93 CQACNDGFY-KSGDA---CSPC--------HESCK-----TCSGG-TASDCTECLTgkalRYGNDGTKG-TCGEGCT 150
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
624-984 3.63e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 3.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  624 RTHIRDIENKLKELLQRIEAANRKTNEASEL--NKNNAKRLARVQTYSAEIKnsryiIDNQNFNSTQLLKEANKNLintk 701
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKEleELEEELEQLRKELEELSRQ-----ISALRKDLARLEAEVEQLE---- 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  702 inyDDLTNLLIDLrngSNYLEEFEGVLWRLNIeykdkfvkrAHDHAMELMRESIRLESLFNKTRDVAVGPLQAAQAYQRI 781
Cdd:TIGR02168  747 ---ERIAQLSKEL---TELEAEIEELEERLEE---------AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  782 VDALlsAEEAAKNASLAAETAFKVAypgDPDKSLVRRATQSLRKSEELhskgEELKMTVGQQFSELDKQRSALGTAKGIL 861
Cdd:TIGR02168  812 LTLL--NEEAANLRERLESLERRIA---ATERRLEDLEEQIEELSEDI----ESLAAEIEELEELIEELESELEALLNER 882
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  862 GVTDDRINGLSTLMETQlstsiSTDIQEVLDRTEETYSNVQKTLDHINAIHMNLTIIReralelSRIDasllyEIRETIS 941
Cdd:TIGR02168  883 ASLEEALALLRSELEEL-----SEELRELESKRSELRRELEELREKLAQLELRLEGLE------VRID-----NLQERLS 946
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 2068726809  942 TGESHTMKGIRKANNLrktgdrIENYSNDLRERIEALKRKIKQ 984
Cdd:TIGR02168  947 EEYSLTLEEAEALENK------IEDDEEEARRRLKRLENKIKE 983
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
505-703 3.64e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 45.33  E-value: 3.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  505 DYYSKDLKQRAEQLEAAARETYPPTAKLRLEAQSILDILNGLYTQIDETIA---------YLKNYAIGETPSISIGGAMM 575
Cdd:COG5185    253 DKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKsidikkateSLEEQLAAAEAEQELEESKR 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  576 EAEK-ILKEIQKRNFTKNDAEAKIELSKAHI--------LLKRIMKMDQEHPLIEAGRTHI----RDIENKLKELLQ--- 639
Cdd:COG5185    333 ETETgIQNLTAEIEQGQESLTENLEAIKEEIenivgeveLSKSSEELDSFKDTIESTKESLdeipQNQRGYAQEILAtle 412
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068726809  640 ---------------RIEAANRKTNEASELNKNNAKRLARVQTYSAEIKNSRYIIDNQNFNSTQLLKEANKNLINTKIN 703
Cdd:COG5185    413 dtlkaadrqieelqrQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIE 491
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
509-653 1.10e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.36  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  509 KDLKQRAEQLEAAARETYPPTAKLRLEAQSILDILNGLYTQIDEtiaYLKNYAIGETPSISIGGAMMEAEKILKEIQKRN 588
Cdd:COG1340     53 KELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDE---LRKELAELNKAGGSIDKLRKEIERLEWRQQTEV 129
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  589 FTKnDAEAKI-----ELSKahiLLKRIMKMDQEHplieagrTHIRDIENKLKELLQRIEAANRKTNEASE 653
Cdd:COG1340    130 LSP-EEEKELvekikELEK---ELEKAKKALEKN-------EKLKELRAELKELRKEAEEIHKKIKELAE 188
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
576-716 2.58e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.70  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  576 EAEKILKEIQKRNFTKNDAEAKIELSKAHILLKRIMKMDQEHPLIEAGRTHIRDIENKLKellqrieaaNRKTNEASELN 655
Cdd:TIGR04523  172 ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLK---------DNIEKKQQEIN 242
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068726809  656 KNNAKrLARVQTYSAEIKNSRYIIDNQNFNSTQLLKEANKNLINTKINYDDLTNLLIDLRN 716
Cdd:TIGR04523  243 EKTTE-ISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN 302
TNFRSF cd00185
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) ...
297-391 5.21e-03

Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) interactions with TNF superfamily (TNFSF) ligands (TNFL) control key cellular processes such as differentiation, proliferation, apoptosis, and cell growth. Dysregulation of these pathways has been shown to result in a wide range of pathological conditions, including autoimmune diseases, inflammation, cancer, and viral infection. There are 29 very diverse family members of TNFRSF reported in humans: 22 are type I transmembrane receptors (single pass with the N terminus on extracellular side of the cell membrane) and have a clear signal peptide; the remaining 7 members are either type III transmembrane receptors (single pass with the N terminus on extracellular side of the membrane but no signal sequence; TNFR13B, TNFR13C, TNFR17, and XEDAR), or attached to the membrane via a glycosylphosphatidylinositol (GPI) linker (TNFR10C), or secreted as soluble receptors (TNFR11B and TNFR6B). All TNFRs contain relatively short cysteine-rich domains (CRDs) in the ectodomain, and are involved in interaction with the TNF homology domain (THD) of their ligands. TNFRs often have multiple CRDs (between one and six), with the most frequent configurations of three or four copies; most CRDs possess three disulfide bridges, but could have between one and four. Localized or genome-wide duplication and evolution of the TNFRSF members appear to have paralleled the emergence of the adaptive immune system; teleosts (i.e. ray-finned, bony fish), which possess an immune system with B and T cells, possess primary and secondary lymphoid organs, and are capable of adaptive responses to pathogens also display several characteristics that are different from the mammalian immune system, making teleost TNFSF orthologs and paralogs of interest to better understand immune system evolution and the immunological pathways elicited to pathogens.


Pssm-ID: 276900 [Multi-domain]  Cd Length: 87  Bit Score: 37.96  E-value: 5.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  297 CDAETGVCENCRDHTMGDhCEVCATGYY-GNPARE-RCKPCA-CPSLEQNFAETCqadryagyichcrTGYTGAKCnRCD 373
Cdd:cd00185      5 CPPGEYLSSDCTATTDTV-CSPCPPGTYsESWNSLsKCLPCTtCGGGNQVEKTPC-------------TATDNRCC-TCK 69
                           90
                   ....*....|....*...
gi 2068726809  374 HGYYGRPSQPRGYCRPCD 391
Cdd:cd00185     70 PGFYCDEGTNVEECKPCT 87
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
547-751 7.43e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 41.74  E-value: 7.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  547 YTQIDETIAYLKN-YAIGETPSI-----SIGGAMMEAE----KILKEIQKRNFTKNDAEAKIELSKAHIllKRIM----- 611
Cdd:PTZ00440  1274 NNKMENALHEIKNmYEFLISIDSekilkEILNSTKKAEefsnDAKKELEKTDNLIKQVEAKIEQAKEHK--NKIYgsled 1351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  612 -KMDQEHPLIEAGRTHIRDIENKLKELLQRIEAANrktnEASELNKNNAKRlarvQTYSAEIKNSRYII---DNQNFN-- 685
Cdd:PTZ00440  1352 kQIDDEIKKIEQIKEEISNKRKEINKYLSNIKSNK----EKCDLHVRNASR----GKDKIDFLNKHEAIepsNSKEVNii 1423
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068726809  686 --------STQLLKEANKNLINTKINYDDLTNLLIDLRNGSNYLEefegvlwRLNIEYKDKFVKRAHDHAMELM 751
Cdd:PTZ00440  1424 kitdninkCKQYSNEAMETENKADENNDSIIKYEKEITNILNNSS-------ILGKKTKLEKKKKEATNIMDDI 1490
IlvC pfam01450
Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase ...
518-625 8.94e-03

Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine.


Pssm-ID: 460215 [Multi-domain]  Cd Length: 138  Bit Score: 38.60  E-value: 8.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068726809  518 LEAAARET-----YPP-TAKLRL--EAQSILDI-----LNGLYTQIDETIAYlknyaiGET---PSIsIGGAMMEA-EKI 580
Cdd:pfam01450   22 LVKAGFETlveagYQPeAAYFEClhELKLIVDLiyeggIAGMRYSISDTAEY------GDLtrgPRV-IYDATKELmKEI 94
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2068726809  581 LKEIQKRNFTKNDAEAKIELSKAhilLKRIMKMDQEHPLIEAGRT 625
Cdd:pfam01450   95 LDEIQSGEFAKEWILEYQAGRPE---LKALRREEAEHPIEKVGKE 136
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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